1s7f

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(New page: 200px<br /><applet load="1s7f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s7f, resolution 2.0&Aring;" /> '''RimL- Ribosomal L7/L1...)
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[[Image:1s7f.gif|left|200px]]<br /><applet load="1s7f" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1s7f, resolution 2.0&Aring;" />
caption="1s7f, resolution 2.0&Aring;" />
'''RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase crystal form I (apo)'''<br />
'''RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase crystal form I (apo)'''<br />
==Overview==
==Overview==
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RimL is responsible for converting the prokaryotic ribosomal protein from, L12 to L7 by acetylation of its N-terminal amino group. We demonstrate, that purified RimL is capable of posttranslationally acetylating L12, exhibiting a V(max) of 21 min(-1). We have also determined the, apostructure of RimL from Salmonella typhimurium and its complex with, coenzyme A, revealing a homodimeric oligomer with structural similarity to, other Gcn5-related N-acetyltransferase superfamily members. A large, central trough located at the dimer interface provides sufficient room to, bind both L12 N-terminal helices. Structural and biochemical analysis, indicates that RimL proceeds by single-step transfer rather than a, covalent-enzyme intermediate. This is the first structure of a, Gcn5-related N-acetyltransferase family member with demonstrated activity, toward a protein N(alpha)-amino group and is a first step toward, understanding the molecular basis for N(alpha)acetylation and its function, in cellular regulation.
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RimL is responsible for converting the prokaryotic ribosomal protein from L12 to L7 by acetylation of its N-terminal amino group. We demonstrate that purified RimL is capable of posttranslationally acetylating L12, exhibiting a V(max) of 21 min(-1). We have also determined the apostructure of RimL from Salmonella typhimurium and its complex with coenzyme A, revealing a homodimeric oligomer with structural similarity to other Gcn5-related N-acetyltransferase superfamily members. A large central trough located at the dimer interface provides sufficient room to bind both L12 N-terminal helices. Structural and biochemical analysis indicates that RimL proceeds by single-step transfer rather than a covalent-enzyme intermediate. This is the first structure of a Gcn5-related N-acetyltransferase family member with demonstrated activity toward a protein N(alpha)-amino group and is a first step toward understanding the molecular basis for N(alpha)acetylation and its function in cellular regulation.
==About this Structure==
==About this Structure==
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1S7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_lt2 Salmonella typhimurium lt2] with CL and MLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S7F OCA].
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1S7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium_lt2 Salmonella typhimurium lt2] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=MLA:'>MLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S7F OCA].
==Reference==
==Reference==
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[[Category: Salmonella typhimurium lt2]]
[[Category: Salmonella typhimurium lt2]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Blanchard, J.S.]]
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[[Category: Blanchard, J S.]]
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[[Category: Carvalho, L.P.de.]]
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[[Category: Carvalho, L P.de.]]
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[[Category: Roderick, S.L.]]
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[[Category: Roderick, S L.]]
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[[Category: Vetting, M.W.]]
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[[Category: Vetting, M W.]]
[[Category: CL]]
[[Category: CL]]
[[Category: MLA]]
[[Category: MLA]]
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[[Category: l7/l12]]
[[Category: l7/l12]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:01:24 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:44 2008''

Revision as of 12:58, 21 February 2008


1s7f, resolution 2.0Å

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RimL- Ribosomal L7/L12 alpha-N-protein acetyltransferase crystal form I (apo)

Overview

RimL is responsible for converting the prokaryotic ribosomal protein from L12 to L7 by acetylation of its N-terminal amino group. We demonstrate that purified RimL is capable of posttranslationally acetylating L12, exhibiting a V(max) of 21 min(-1). We have also determined the apostructure of RimL from Salmonella typhimurium and its complex with coenzyme A, revealing a homodimeric oligomer with structural similarity to other Gcn5-related N-acetyltransferase superfamily members. A large central trough located at the dimer interface provides sufficient room to bind both L12 N-terminal helices. Structural and biochemical analysis indicates that RimL proceeds by single-step transfer rather than a covalent-enzyme intermediate. This is the first structure of a Gcn5-related N-acetyltransferase family member with demonstrated activity toward a protein N(alpha)-amino group and is a first step toward understanding the molecular basis for N(alpha)acetylation and its function in cellular regulation.

About this Structure

1S7F is a Single protein structure of sequence from Salmonella typhimurium lt2 with and as ligands. Full crystallographic information is available from OCA.

Reference

A novel dimeric structure of the RimL Nalpha-acetyltransferase from Salmonella typhimurium., Vetting MW, de Carvalho LP, Roderick SL, Blanchard JS, J Biol Chem. 2005 Jun 10;280(23):22108-14. Epub 2005 Apr 6. PMID:15817456

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